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J. Biol. Chem., Vol. 280, Issue 11, 10141-10148, March 18, 2005

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p125 Is Localized in Endoplasmic Reticulum Exit Sites and Involved in Their Organization^*

Wakako Shimoi, Ichiko Ezawa, Koji Nakamoto, Shihoko Uesaki, Gavin Gabreski, Meir Aridor, Akitsugu Yamamoto¶, Masami Nagahama, Mitsuo Tagaya, and Katsuko Tani||

From the School of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan, the Department of Cell Biology and Physiology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261, and the ^¶Department of Cell Biology, Nagahama Institute of Bio-Science and Technology, Nagahama, Shiga 526-0829, Japan

Transport vesicles coated with the COPII complex, which is assembled from Sar1p, Sec23p-Sec24p, and Sec13p-Sec31p, are involved in protein export from the endoplasmic reticulum (ER). We previously identified and characterized a novel Sec23p-interacting protein, p125, that is only expressed in mammals and exhibits sequence homology with phosphatidic acid-preferring phospholipase A₁ (PA-PLA₁). In this study, we examined the localization and function of p125 in detail. By using immunofluorescence and electron microscopy, we found that p125 is principally localized in ER exit sites where COPII-coated vesicles are produced. Analyses of chimeric proteins comprising p125 and two other members of the mammalian PA-PLA₁ family (PA-PLA₁ and KIAA0725p) showed that, for localization to ER exit sites, the p125-specific N-terminal region is critical, and the putative lipase domain is interchangeable with KIAA0725p but not with PA-PLA₁. RNA interference-mediated depletion of p125 affected the organization of ER exit sites. The structure of the cis-Golgi compartment was also substantially disturbed, whereas the medial-Golgi was not. Protein export from the ER occurred without a significant delay in p125-depleted cells. Our study suggests that p125 is a mammalian-specific component of ER exit sites and participates in the organization of this compartment.

Received for publication, August 23, 2004 , and in revised form, December 8, 2004.

^* This work was supported in part by Grants-in-aid for Scientific Research 15570165 (to K. T.) and 16044242, 16370089, and 16657309 (to M. T.) from the Ministry of Education, Science, Sports and Culture of Japan and by National Institutes of Health Grant DK062318-01A2 (to M. A.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^|| To whom correspondence should be addressed: School of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan. Tel.: 81-426-76-7110; Fax: 81-426-76-8866; E-mail: tani{at}ls.toyaku.ac.jp.

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